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Database: UniProt
Entry: X7EAR6_9RHOB
LinkDB: X7EAR6_9RHOB
Original site: X7EAR6_9RHOB 
ID   X7EAR6_9RHOB            Unreviewed;       376 AA.
AC   X7EAR6;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   SubName: Full=Alpha-hydroxy acid dehydrogenase {ECO:0000313|EMBL:ETX13027.1};
GN   ORFNames=OCH239_14770 {ECO:0000313|EMBL:ETX13027.1};
OS   Roseivivax halodurans JCM 10272.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Roseivivax.
OX   NCBI_TaxID=1449350 {ECO:0000313|EMBL:ETX13027.1, ECO:0000313|Proteomes:UP000022447};
RN   [1] {ECO:0000313|EMBL:ETX13027.1, ECO:0000313|Proteomes:UP000022447}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 10272 {ECO:0000313|EMBL:ETX13027.1,
RC   ECO:0000313|Proteomes:UP000022447};
RA   Lai Q., Li G., Shao Z.;
RT   "Roseivivax halodurans JCM 10272 Genome Sequencing.";
RL   Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000256|ARBA:ARBA00001917};
CC   -!- SIMILARITY: Belongs to the FMN-dependent alpha-hydroxy acid
CC       dehydrogenase family. {ECO:0000256|ARBA:ARBA00024042}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ETX13027.1}.
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DR   EMBL; JALZ01000040; ETX13027.1; -; Genomic_DNA.
DR   RefSeq; WP_037266125.1; NZ_JALZ01000040.1.
DR   AlphaFoldDB; X7EAR6; -.
DR   STRING; 1449350.OCH239_14770; -.
DR   PATRIC; fig|1449350.3.peg.3795; -.
DR   eggNOG; COG1304; Bacteria.
DR   OrthoDB; 9770452at2; -.
DR   Proteomes; UP000022447; Unassembled WGS sequence.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   CDD; cd02809; alpha_hydroxyacid_oxid_FMN; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR012133; Alpha-hydoxy_acid_DH_FMN.
DR   InterPro; IPR000262; FMN-dep_DH.
DR   InterPro; IPR037396; FMN_HAD.
DR   InterPro; IPR008259; FMN_hydac_DH_AS.
DR   PANTHER; PTHR10578:SF107; FMN HYDROXY ACID DEHYDROGENASE DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR10578; S -2-HYDROXY-ACID OXIDASE-RELATED; 1.
DR   Pfam; PF01070; FMN_dh; 1.
DR   PIRSF; PIRSF000138; Al-hdrx_acd_dh; 1.
DR   SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
DR   PROSITE; PS00557; FMN_HYDROXY_ACID_DH_1; 1.
DR   PROSITE; PS51349; FMN_HYDROXY_ACID_DH_2; 1.
PE   3: Inferred from homology;
KW   Flavoprotein {ECO:0000256|PIRSR:PIRSR000138-2};
KW   FMN {ECO:0000256|PIRSR:PIRSR000138-2};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000022447}.
FT   DOMAIN          1..376
FT                   /note="FMN hydroxy acid dehydrogenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51349"
FT   ACT_SITE        277
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-1"
FT   BINDING         25
FT                   /ligand="glyoxylate"
FT                   /ligand_id="ChEBI:CHEBI:36655"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT   BINDING         79..81
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT   BINDING         108
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT   BINDING         129
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT   BINDING         131
FT                   /ligand="glyoxylate"
FT                   /ligand_id="ChEBI:CHEBI:36655"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT   BINDING         157
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT   BINDING         166
FT                   /ligand="glyoxylate"
FT                   /ligand_id="ChEBI:CHEBI:36655"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT   BINDING         253
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT   BINDING         275
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT   BINDING         277
FT                   /ligand="glyoxylate"
FT                   /ligand_id="ChEBI:CHEBI:36655"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT   BINDING         280
FT                   /ligand="glyoxylate"
FT                   /ligand_id="ChEBI:CHEBI:36655"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT   BINDING         308..312
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT   BINDING         331..332
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
SQ   SEQUENCE   376 AA;  40321 MW;  E7B72C43D6E2A49C CRC64;
     MAGVISADDL RRRARRKLPR FAFDYIDGGA GTEAGLARNR AAWLGETLQP KVLVNSDRAL
     PTERSFLGRR WAMPIGIPPI GLAGLAWPEV DLILASAAEA AGIPYVASTP ATVSLERLKS
     AAPTSGWFQL YVGKSEEITD DLIRRARDAG YETLVVTADV PRPGIRLRDV RNGFSLPLKA
     TPRMAADLAL HPAWAIRTFR AGAPRFANLE RYAAPGTGAQ SLAKLMAGQS SGRLDWTLFR
     RIREQWPGRL ILKGVTSAPD AAQAADLGAD AIWVSNHGGR QLDSAPATRD ALPAIRKAVP
     EDFPLAVDGG LRGGEDVLKA LVAGADFAFV GRPFLYSVAA LGAEGPTRYI ETLAAQLDNA
     MAQIGWTDLD RSPRDV
//
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